1gq8 Summary



The structure was published by Johansson, K., El-Ahmad, M., Friemann, R., Jornvall, H., Markovic, O., and Eklund, H., in 2002 in a paper entitled "Crystal Structure of Plant Pectin Methylesterase" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.75 Å and deposited in 2001.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of PECTINESTERASE. This molecule has the UniProt identifier P83218 (PME_DAUCA)search. The sample contained 319 residues which is 100% of the natural sequence. Out of 319 residues 319 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A PECTINESTERASE P83218 (2-319) (PME_DAUCA)search Daucus carotasearch 100% 319 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P83218 (2 - 319) PECTINESTERASE Daucus carota

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P83218) Pectin methylesterasesearch Single-stranded right-handed beta-helix, Pectin lyase-likesearch PF01095: Pectinesterasesearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A (P83218) hydrolase activitysearch pectinesterase activitysearch aspartyl esterase activitysearch cell wallsearch extracellular regionsearch cell wall modificationsearch pectin catabolic processsearch

Chain InterPro annotation
A Pectinesterase, catalyticsearch Pectin lyase fold/virulence factorsearch Pectin lyase foldsearch Pectinesterase, active sitesearch